ID D5G9C6_TUBMM Unreviewed; 410 AA.
AC D5G9C6;
DT 15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT 15-JUN-2010, sequence version 1.
DT 06-MAR-2013, entry version 17.
DE RecName: Full=Aspartate aminotransferase;
DE EC=2.6.1.1;
GN ORFNames=GSTUM_00003243001;
OS Tuber melanosporum (strain Mel28) (Perigord black truffle).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Pezizomycetes;
OC Pezizales; Tuberaceae; Tuber.
OX NCBI_TaxID=656061;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Mel28;
RX PubMed=20348908; DOI=10.1038/nature08867;
RA Martin F., Kohler A., Murat C., Balestrini R., Coutinho P.M.,
RA Jaillon O., Montanini B., Morin E., Noel B., Percudani R., Porcel B.,
RA Rubini A., Amicucci A., Amselem J., Anthouard V., Arcioni S.,
RA Artiguenave F., Aury J.M., Ballario P., Bolchi A., Brenna A., Brun A.,
RA Buee M., Cantarel B., Chevalier G., Couloux A., Da Silva C.,
RA Denoeud F., Duplessis S., Ghignone S., Hilselberger B., Iotti M.,
RA Marcais B., Mello A., Miranda M., Pacioni G., Quesneville H.,
RA Riccioni C., Ruotolo R., Splivallo R., Stocchi V., Tisserant E.,
RA Viscomi A.R., Zambonelli A., Zampieri E., Henrissat B., Lebrun M.H.,
RA Paolocci F., Bonfante P., Ottonello S., Wincker P.;
RT "Perigord black truffle genome uncovers evolutionary origins and
RT mechanisms of symbiosis.";
RL Nature 464:1033-1038(2010).
CC -!- CATALYTIC ACTIVITY: L-aspartate + 2-oxoglutarate = oxaloacetate +
CC L-glutamate.
CC -!- COFACTOR: Pyridoxal phosphate (By similarity).
CC -!- SUBUNIT: Homodimer (By similarity).
CC -!- MISCELLANEOUS: In eukaryotes there are cytoplasmic, mitochondrial
CC and chloroplastic isozymes (By similarity).
CC -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC aminotransferase family.
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DR EMBL; FN430059; CAZ81119.1; -; Genomic_DNA.
DR RefSeq; XP_002836928.1; XM_002836882.1.
DR UniGene; Tme.5522; -.
DR ProteinModelPortal; D5G9C6; -.
DR EnsemblFungi; CAZ81119; CAZ81119; GSTUM_00003243001.
DR GeneID; 9182870; -.
DR KEGG; tml:GSTUM_00003243001; -.
DR KO; K14455; -.
DR GO; GO:0004069; F:L-aspartate:2-oxoglutarate aminotransferase activity; IEA:EC.
DR GO; GO:0080130; F:L-phenylalanine:2-oxoglutarate aminotransferase activity; IEA:EC.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR GO; GO:0006520; P:cellular amino acid metabolic process; IEA:InterPro.
DR Gene3D; 3.40.640.10; -; 1.
DR InterPro; IPR004839; Aminotransferase_I/II.
DR InterPro; IPR000796; Asp_trans.
DR InterPro; IPR004838; NHTrfase_class1_PyrdxlP-BS.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major_sub1.
DR PANTHER; PTHR11879; PTHR11879; 1.
DR Pfam; PF00155; Aminotran_1_2; 1.
DR PRINTS; PR00799; TRANSAMINASE.
DR SUPFAM; SSF53383; PyrdxlP-dep_Trfase_major; 1.
DR PROSITE; PS00105; AA_TRANSFER_CLASS_1; 1.
PE 3: Inferred from homology;
KW Aminotransferase; Complete proteome; Pyridoxal phosphate;
KW Reference proteome; Transferase.
SQ SEQUENCE 410 AA; 45552 MW; 6CD5DFFBAC150F33 CRC64;
MLSARIFFPC RSCKHLEQCY SRATCATGIT EAYKADKFDR KVNLGVGAYR DDKGNPYVLP
SVRAAEERIL MKGLDKEYAA ITGVLSFTKA AIELAYGKPS HALDRIAATQ SISGTGALRI
GGAFLERFYP FSKTVYLPTP SWANHAAIMK DSKINVKSYR YYNSQTIRLD IDGLLEDIGN
APKNSIFLFH ACAHNPTGVD PTPEQWRAIS EAVKSCGHFP FFDMAYQGFA SGDTNKDAYA
LRYFIEQGHP VALSQSFAKN MGLYGERVGV FSLLAESAEE KRRLDSQIKI LVRPLYSNPP
VNGARIASEI LNDLTLRKQW LSEVRGMADR IISMRAALKT NLEEIGSKHD WSHITSQIGM
FAYTGLRPEQ VDRLAKEFSI YGTKDGRISV AGITSDNVKY LAESIHKVTA
//
